Association of RNA with the uracil-DNA-degrading factor has major conformational effects and is potentially involved in protein folding

FEBS Journal

Volumn 278, Issue 2, 2011, Pages 295-315

  Bekesi, Angela ^a   Pukancsik, Maria ^a   Haasz, Peter ^a   Felfoldi, Lilla ^a   Leveles, Ibolya ^a   Muha, Villo ^a   Hunyadi Gulyas, Eva ^a   Erdei, Anna ^b   Medzihradszky, Katalin F ^a,c   Vertessy, Beata G ^a,d  

^a INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^b EÖTVÖS LORÁND UNIVERSITY   (Hungary)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d BUDAPEST UNIVERSITY OF TECHNOLOGY AND ECONOMICS   (Hungary)

Author keywords

conformational states; cotranslational folding; RNA binding; RNA assisted folding; uracil DNA degrading factor

Indexed keywords

DROSOPHILA PROTEIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; NICKEL; RIBOSOME RNA; RNA; UNCLASSIFIED DRUG; URACIL DNA DEGRADING FACTOR;

AFFINITY CHROMATOGRAPHY; ALPHA HELIX; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTALLIZATION; DNA BINDING; DNA DEGRADATION; GEL MOBILITY SHIFT ASSAY; GEL PERMEATION CHROMATOGRAPHY; HYDROPHOBICITY; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN STABILITY; PROTEIN STRUCTURE; REAL TIME POLYMERASE CHAIN REACTION; RNA BINDING; RNA CLEAVAGE; RNA CONFORMATION;

ANIMALS; CIRCULAR DICHROISM; DNA; DNA, SINGLE-STRANDED; DNA-BINDING PROTEINS; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; ELECTROPHORETIC MOBILITY SHIFT ASSAY; ENDOPEPTIDASES; FLUORESCENT DYES; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MODELS, MOLECULAR; OLIGODEOXYRIBONUCLEOTIDES; OLIGORIBONUCLEOTIDES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN UNFOLDING; PUPA; RECOMBINANT PROTEINS; RIBONUCLEASES; RNA; RNA, DOUBLE-STRANDED; RNA, MESSENGER; RNA, RIBOSOMAL, 16S; RNA, RIBOSOMAL, 23S; SPECTROMETRY, FLUORESCENCE; SURFACE PROPERTIES; TEMPERATURE; TRANSITION TEMPERATURE;

DROSOPHILA MELANOGASTER; HEXAPODA;

EID: 78651090558     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2010.07951.x     Document Type: Article

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